Analytical Data
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Gene name
pPLA2
- Application
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Alternative Names
pPLA2；PLA2；PLA2A；PPLA2；Phospholipase A2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04054
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Expression Region
23-148aa
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AA Sequence
AVWQFRKM IKCVIPGSDP FLEYNNYGCY CGLGGSGTPV DELDKCCQTH DNCYDQAKKL DSCKFLLDNP YTHTYSYSCS GSAITCSSKN KECEAFICNC DRNAAICFSK APYNKAHKNL DTKKYCQS
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of recombinant phospholipase A2 (PLA2) has garnered significant attention due to its crucial role in various biological processes and its potential applications in biotechnology and medicine. PLA2 enzymes are widely distributed in nature, involved in the hydrolysis of phospholipids to release fatty acids and lysolipids, which are pivotal in cell membrane dynamics, signaling pathways, and inflammatory responses. The principal focus has been on secreted PLA2 (sPLA2) and its isoforms, which have been implicated in pathological conditions such as cardiovascular diseases, neurodegenerative disorders, and cancer. By utilizing recombinant DNA technologies, researchers can produce sPLA2 proteins with enhanced stability, activity, and specificity. This enables detailed studies of their structural and functional properties, as well as the development of PLA2 inhibitors as potential therapeutic agents. Moreover, the recombinant proteins can serve as valuable research tools for studying membrane interactions and enzymatic mechanisms. As a result, the exploration of PLA2 not only aids in understanding fundamental biological processes but also paves the way for innovative treatments targeting PLA2-related diseases, emphasizing the importance of continued research and development in this field.
